메뉴 건너뛰기




Volumn 23, Issue 11, 2012, Pages 2020-2030

Structural and energetic effects in the molecular recognition of acetylated amino acids by 18-crown-6

Author keywords

18 Crown 6; Acetylated amino acids; Binding affinities; Collision induced dissociation; Hydrogen bonding interactions; Molecular recognition

Indexed keywords

18-CROWN-6; AMINO GROUP; BINDING AFFINITIES; BOND DISSOCIATION ENERGIES; COLLISION-INDUCED DISSOCIATION; CROSS SECTION; DISSOCIATION PATHWAYS; ELECTRONIC STRUCTURE CALCULATIONS; ENERGETIC EFFECT; HYDROGEN BONDING INTERACTIONS; INTERNAL ENERGIES; MULTIPLE COLLISIONS; N-TERMINALS; PROTONATED; SEQUENTIAL DISSOCIATION; SIDE-CHAINS; TANDEM MASS SPECTROMETRY TECHNIQUES; UNIMOLECULAR DISSOCIATION;

EID: 84868257020     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-012-0466-z     Document Type: Article
Times cited : (12)

References (57)
  • 1
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith, D.L., Deng, Y., Zhang, Z.: Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass Spectrom. 32, 135-146 (1997)
    • (1997) J. Mass Spectrom. , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 2
    • 0035326304 scopus 로고    scopus 로고
    • A powerful new approach that goes beyond deciphering protein structures
    • Engen, J.R., Smith, D.L.: A powerful new approach that goes beyond deciphering protein structures. Anal. Chem. 73, 256A-265A (2001)
    • (2001) Anal. Chem. , vol.73
    • Engen, J.R.1    Smith, D.L.2
  • 3
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamics by mass spectrometry
    • Kaltashov, I.A., Eyles, S.: Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom. Rev. 21, 37-71 (2002)
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.2
  • 5
    • 3342925849 scopus 로고    scopus 로고
    • Methods to study protein dynamics and folding by mass spectrometry
    • Eyles, S.J., Kaltashov, I.A.: Methods to study protein dynamics and folding by mass spectrometry. Methods 34, 88-99 (2004)
    • (2004) Methods , vol.34 , pp. 88-99
    • Eyles, S.J.1    Kaltashov, I.A.2
  • 6
    • 2342485044 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry for investigating protein-ligand interactions
    • Garcia, R.A., Pantazatos, D., Villarreal, F.J.: Hydrogen/deuterium exchange mass spectrometry for investigating protein-ligand interactions. Assay Drug Dev. Technol. 2, 81-91 (2004)
    • (2004) Assay Drug Dev. Technol. , vol.2 , pp. 81-91
    • Garcia, R.A.1    Pantazatos, D.2    Villarreal, F.J.3
  • 7
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz, A.: Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Spectrom. 38, 1225-1237 (2003)
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 8
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner, J.: New photolabeling and crosslinking methods. Annu. Rev. Biochem. 62, 483-514 (1993)
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 483-514
    • Brunner, J.1
  • 9
    • 8644282069 scopus 로고    scopus 로고
    • Chemical cross-linking and protein-protein interactions: A review with illustrative protocols
    • Kluger, R., Alagic, A.: Chemical cross-linking and protein-protein interactions: a review with illustrative protocols. Bioorg. Chem. 32, 451-472 (2004)
    • (2004) Bioorg. Chem. , vol.32 , pp. 451-472
    • Kluger, R.1    Alagic, A.2
  • 10
    • 3442888009 scopus 로고    scopus 로고
    • New chemical crosslinking methods for the identification of transient protein-protein interactions with multiprotein complexes
    • Melcher, K.: New chemical crosslinking methods for the identification of transient protein-protein interactions with multiprotein complexes. Curr. Prot. Pept. Sci. 5, 287-296 (2004)
    • (2004) Curr. Prot. Pept. Sci. , vol.5 , pp. 287-296
    • Melcher, K.1
  • 11
    • 15944384662 scopus 로고    scopus 로고
    • Techniques: Oxidative cross-linking as an emergent tool for the analysis of receptor-mediated signaling events
    • Kodadek, T., Duroux-Richard, I., Bonnafous, J.C.: Techniques: oxidative cross-linking as an emergent tool for the analysis of receptor-mediated signaling events. Trends Pharmacol. Sci. 26, 210-217 (2005)
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 210-217
    • Kodadek, T.1    Duroux-Richard, I.2    Bonnafous, J.C.3
  • 12
    • 0042349690 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for protein structural modeling
    • Back, J.W., de Jong, L., Muijsers, A.O., de Koster, C.G.: Chemical cross-linking and mass spectrometry for protein structural modeling. J. Mol. Biol. 331, 303-313 (2003)
    • (2003) J. Mol. Biol. , vol.331 , pp. 303-313
    • Back, J.W.1    De Jong, L.2    Muijsers, A.O.3    De Koster, C.G.4
  • 13
    • 13844299576 scopus 로고    scopus 로고
    • Mapping protein-protein interactions by bioinformatics and cross-linking
    • Friedhoff, P.: Mapping protein-protein interactions by bioinformatics and cross-linking. Anal. Bioanal. Chem. 381, 78-80 (2005)
    • (2005) Anal. Bioanal. Chem. , vol.381 , pp. 78-80
    • Friedhoff, P.1
  • 14
    • 22644437896 scopus 로고    scopus 로고
    • Identification and mapping of protein-protein interactions by a combination of cross-linking, cleavage, and proteomics
    • Trakselis, M.A., Alley, S.C., Ishmael, F.T.: Identification and mapping of protein-protein interactions by a combination of cross-linking, cleavage, and proteomics. Bioconjug. Chem. 16, 741-750 (2005)
    • (2005) Bioconjug. Chem. , vol.16 , pp. 741-750
    • Trakselis, M.A.1    Alley, S.C.2    Ishmael, F.T.3
  • 16
    • 0035860265 scopus 로고    scopus 로고
    • Site specific sequestering and stabilization of charge in peptides by supramolecular adduct formation with 18-crown-6 ether by way of electrospray ionization
    • Julian, R.R., Beauchamp, J.L.: Site specific sequestering and stabilization of charge in peptides by supramolecular adduct formation with 18-crown-6 ether by way of electrospray ionization. Int. J. Mass Spectrom. 210/211, 613-623 (2001)
    • (2001) Int. J. Mass Spectrom. , vol.210-211 , pp. 613-623
    • Julian, R.R.1    Beauchamp, J.L.2
  • 17
    • 0036582779 scopus 로고    scopus 로고
    • The unusually high proton affinity of aza-18-crown-6 ether: Implications for the molecular recognition of lysine in peptides by lariat crown ethers
    • Julian, R.R., Beauchamp, J.L.: The unusually high proton affinity of Aza-18-crown-6 ether: Implications for the molecular recognition of lysine in peptides by lariat crown ethers. J. Am. Soc. Mass Spectrom. 13, 493-498 (2002)
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 493-498
    • Julian, R.R.1    Beauchamp, J.L.2
  • 18
    • 1642462451 scopus 로고    scopus 로고
    • Selective molecular recognition of arginine by anionic salt bridge formation with bis-phosphate crown ethers: Implications for gas phase peptide acidity from adduct dissociation
    • Julian, R.R., Beauchamp, J.L.: Selective molecular recognition of arginine by anionic salt bridge formation with Bis-phosphate crown ethers: Implications for Gas phase peptide acidity from adduct dissociation. J. Am. Soc. Mass Spectrom. 15, 616-624 (2004)
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 616-624
    • Julian, R.R.1    Beauchamp, J.L.2
  • 19
    • 0037105298 scopus 로고    scopus 로고
    • Molecular recognition of arginine in small peptides by supramolecular complexation with dibenzo-30-crown-10 ether
    • Julian, R.R., Akin, M., May, J.A., Stoltz, B.M., Beauchamp, J.L.: Molecular recognition of arginine in small peptides by supramolecular complexation with dibenzo-30-crown-10 ether. Int. J. Mass Spectrom. 220, 87-96 (2002)
    • (2002) Int. J. Mass Spectrom. , vol.220 , pp. 87-96
    • Julian, R.R.1    Akin, M.2    May, J.A.3    Stoltz, B.M.4    Beauchamp, J.L.5
  • 20
    • 0042707487 scopus 로고    scopus 로고
    • Biomimetic approaches to gas phase peptide chemistry: Combining selective binding motifs with reactive carbene precursors to form molecular mousetraps
    • Julian, R.R., May, J.A., Stoltz, B.M., Beauchamp, J.L.: Biomimetic approaches to gas phase peptide chemistry: Combining selective binding motifs with reactive carbene precursors to form molecular mousetraps. Int. J. Mass Spectrom. 228, 851-864 (2003)
    • (2003) Int. J. Mass Spectrom. , vol.228 , pp. 851-864
    • Julian, R.R.1    May, J.A.2    Stoltz, B.M.3    Beauchamp, J.L.4
  • 21
    • 33747882757 scopus 로고    scopus 로고
    • Using ESI-MS to probe protein structure by site-specific noncovalent attachment of 18-crown-6
    • Ly, T., Julian, R.R.: Using ESI-MS to probe protein structure by site-specific noncovalent attachment of 18-crown-6. J. Am. Soc. Mass Spectrom. 17, 1209-1215 (2006)
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1209-1215
    • Ly, T.1    Julian, R.R.2
  • 22
    • 55149085458 scopus 로고    scopus 로고
    • Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry
    • Ly, T., Julian, R.R.: Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry. J. Am. Soc. Mass Spectrom. 19, 1663-1672 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1663-1672
    • Ly, T.1    Julian, R.R.2
  • 23
    • 43949144960 scopus 로고    scopus 로고
    • Exploring the mechanism of selective noncovalent adduct protein probing mass spectrometry utilizing site-directed mutagenesis to examine ubiquitin
    • Liu, Z., Cheng, S., Gallie, D.R., Julian, R.R.: Exploring the mechanism of selective noncovalent adduct protein probing mass spectrometry utilizing site-directed mutagenesis to examine ubiquitin. Anal. Chem. 80, 3846-3852 (2008)
    • (2008) Anal. Chem. , vol.80 , pp. 3846-3852
    • Liu, Z.1    Cheng, S.2    Gallie, D.R.3    Julian, R.R.4
  • 24
    • 46849114907 scopus 로고    scopus 로고
    • Surveying ubiquitin structure by noncovalent attachment of distance constrained bis(crown) ethers
    • Ly, T., Liu, Z., Pujanauski, B.G., Sarpong, R., Julian, R.R.: Surveying ubiquitin structure by noncovalent attachment of distance constrained Bis(crown) ethers. Anal. Chem. 80, 5059-5064 (2008)
    • (2008) Anal. Chem. , vol.80 , pp. 5059-5064
    • Ly, T.1    Liu, Z.2    Pujanauski, B.G.3    Sarpong, R.4    Julian, R.R.5
  • 25
    • 60649115219 scopus 로고    scopus 로고
    • Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores
    • Yeh, G.K., Sun, Q., Meneses, C., Julian, R.R.: Rapid peptide fragmentation without electrons, collisions, infrared radiation, or native chromophores. J. Am. Soc. Mass Spectrom. 20, 385-393 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 385-393
    • Yeh, G.K.1    Sun, Q.2    Meneses, C.3    Julian, R.R.4
  • 26
    • 77953548631 scopus 로고    scopus 로고
    • Alternate dissociation pathways identified in charge-reduced protein complex ions
    • Pagel, K., Hyung, S.J., Ruotolo, B.T., Robinson, C.V.: Alternate dissociation pathways identified in charge-reduced protein complex ions. Anal. Chem. 82, 5363-5372 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 5363-5372
    • Pagel, K.1    Hyung, S.J.2    Ruotolo, B.T.3    Robinson, C.V.4
  • 27
    • 77955269546 scopus 로고    scopus 로고
    • Extraction and separation of a lysine-rich protein by formation of supramolecule between crown ether and protein in aqueous two-phase system
    • Oshima, T., Suetsugu, A., Baba, Y.: Extraction and separation of a lysine-rich protein by formation of supramolecule between crown ether and protein in aqueous two-phase system. Anal. Chim. Acta 674, 211-219 (2010)
    • (2010) Anal. Chim. Acta , vol.674 , pp. 211-219
    • Oshima, T.1    Suetsugu, A.2    Baba, Y.3
  • 28
    • 0032483698 scopus 로고    scopus 로고
    • Sequence-selective evaluation of peptide side-chain interaction. New artificial receptors for selective recognition in water
    • Hossain, M.A., Schneider, H.J.: Sequence-selective evaluation of peptide side-chain interaction. New artificial receptors for selective recognition in water. J. Am. Chem. Soc. 120, 11208-11209 (1998)
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11208-11209
    • Hossain, M.A.1    Schneider, H.J.2
  • 29
    • 0034228707 scopus 로고    scopus 로고
    • Peptide and protein recognition by designed molecules
    • Peczuh, M.W., Hamilton, A.D.: Peptide and protein recognition by designed molecules. Chem. Rev. 100, 2479-2494 (2000)
    • (2000) Chem. Rev. , vol.100 , pp. 2479-2494
    • Peczuh, M.W.1    Hamilton, A.D.2
  • 30
    • 84863011402 scopus 로고    scopus 로고
    • Structural and energetic effects in the molecular recognition of protonated peptidomimetic bases by 18-crown-6
    • Chen, Y., Rodgers, M.T.: Structural and energetic effects in the molecular recognition of protonated peptidomimetic bases by 18-crown-6. J. Am. Chem. Soc. 134, 2313-2324 (2012)
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2313-2324
    • Chen, Y.1    Rodgers, M.T.2
  • 31
    • 84859357286 scopus 로고    scopus 로고
    • Structural and energetic effects in the molecular recognition of amino acids by 18-crown-6
    • Chen, Y.; Rodgers, M. T.: Structural and energetic effects in the molecular recognition of amino acids by 18-Crown-6. J. Am. Chem. Soc. 134, 5863-5875 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 5863-5875
    • Chen, Y.1    Rodgers, M.T.2
  • 32
    • 0035818138 scopus 로고    scopus 로고
    • Substituent effects in the binding of alkali metal ions to pyridines studied by threshold collision-induced dissociation and ab initio theory: The methylpyridines
    • Rodgers, M.T.: Substituent effects in the binding of alkali metal ions to pyridines studied by threshold collision-induced dissociation and Ab initio theory: The methylpyridines. J. Phys. Chem. A 105, 2374-2383 (2001)
    • (2001) J. Phys. Chem. A , vol.105 , pp. 2374-2383
    • Rodgers, M.T.1
  • 35
    • 0031101986 scopus 로고    scopus 로고
    • Statistical modeling of collision-induced dissociation thresholds
    • Rodgers, M.T., Ervin, K.M., Armentrout, P.B.: Statistical modeling of collision-induced dissociation thresholds. J. Chem. Phys. 106, 4499-4508 (1997)
    • (1997) J. Chem. Phys. , vol.106 , pp. 4499-4508
    • Rodgers, M.T.1    Ervin, K.M.2    Armentrout, P.B.3
  • 38
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A.D.: Density-functional thermochemistry. III. The role of exact exchange. J. Chem. Phys. 98, 5648-5652 (1993)
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 39
    • 0345491105 scopus 로고
    • Development of the colle-salvetti correlation-energy formula into a functional of the electron density
    • Lee, C., Yang, W., Parr, R.G.: Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density. Phys. Rev. B 37, 785-789 (1988)
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 41
    • 84890021933 scopus 로고
    • The calculation of small molecular interactions by the differences of separate total energies
    • Boys, S.F., Bernardi, R.: The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors. Mol. Phys. 19, 553-566 (1970)
    • (1970) Some Procedures with Reduced Errors. Mol. Phys. , vol.19 , pp. 553-566
    • Boys, S.F.1    Bernardi, R.2
  • 43
    • 0001475454 scopus 로고    scopus 로고
    • Toward reliable density functional methods without adjustable parameters: The PBE0 model
    • Adamo, C., Barone, V.: Toward reliable density functional methods without adjustable parameters: The PBE0 model. J. Chem. Phys. 110, 6158-6170 (1999)
    • (1999) J. Chem. Phys. , vol.110 , pp. 6158-6170
    • Adamo, C.1    Barone, V.2
  • 46
    • 0001682728 scopus 로고    scopus 로고
    • 2n+2O, n=1-4. Determined by threshold collision-induced dissociation
    • 2n+2O, n=1-4. Determined by threshold collision-induced dissociation. J. Phys. Chem. A 101, 2614-2625 (1997)
    • (1997) J. Phys. Chem. A , vol.101 , pp. 2614-2625
    • Rodgers, M.T.1    Armentrout, P.B.2
  • 47
    • 0009709120 scopus 로고    scopus 로고
    • Absolute alkali metal ion binding affinities of several azoles determined by threshold collision-induced dissociation
    • 187
    • Rodgers, M.T., Armentrout, P.B.: Absolute alkali metal Ion binding affinities of several azoles determined by threshold collision-induced dissociation. Int. J. Mass Spectrom. 185/186/187, 359-380 (1999)
    • (1999) Int. J. Mass Spectrom. , vol.185-186 , pp. 359-380
    • Rodgers, M.T.1    Armentrout, P.B.2
  • 48
    • 0001242666 scopus 로고    scopus 로고
    • 2n+2O, n=1-4, determined by threshold collision-induced dissociation experiments and ab initio theory
    • 2n+2O, n=1-4, determined by threshold collision-induced dissociation experiments and Ab initio theory. J. Phys. Chem. A 103, 4955-4963 (1999)
    • (1999) J. Phys. Chem. A , vol.103 , pp. 4955-4963
    • Rodgers, M.T.1    Armentrout, P.B.2
  • 49
    • 0034704866 scopus 로고    scopus 로고
    • An absolute sodium cation affinity scale: Threshold collision-induced dissociation experiments and ab initio theory
    • Armentrout, P.B., Rodgers, M.T.: An absolute sodium cation affinity scale: Threshold collision-induced dissociation experiments and ab initio theory. J. Phys. Chem. A 104, 2238-2247 (1999)
    • (1999) J. Phys. Chem. A , vol.104 , pp. 2238-2247
    • Armentrout, P.B.1    Rodgers, M.T.2
  • 50
    • 17144446812 scopus 로고    scopus 로고
    • Absolute alkali metal ion binding affinities of several azines determined by threshold collision-induced dissociation and ab initio theory
    • Amunugama, R., Rodgers, M.T.: Absolute alkali metal Ion binding affinities of several azines determined by threshold collision-induced dissociation and ab initio theory. Int. J. Mass Spectrom. 195/196, 439-457 (2000)
    • (2000) Int. J. Mass Spectrom. , vol.195-196 , pp. 439-457
    • Amunugama, R.1    Rodgers, M.T.2
  • 51
    • 0033824826 scopus 로고    scopus 로고
    • Noncovalent interactions of nucleic acid bases (Uracil, thymine, and adenine) with alkali metal ions. Threshold collision-induced dissociation and theoretical studies
    • Rodgers, M.T., Armentrout, P.B.: Noncovalent interactions of nucleic acid bases (Uracil, Thymine, and Adenine) with alkali metal ions. Threshold collision-induced dissociation and theoretical studies. J. Am. Chem. Soc. 122, 8548-8558 (2000)
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8548-8558
    • Rodgers, M.T.1    Armentrout, P.B.2
  • 52
    • 0001476818 scopus 로고    scopus 로고
    • Statistical modeling of competitive threshold collision-induced dissociation
    • Rodgers, M.T., Armentrout, P.B.: Statistical modeling of competitive threshold collision-induced dissociation. J. Chem. Phys. 109, 1787-1800 (1998)
    • (1998) J. Chem. Phys. , vol.109 , pp. 1787-1800
    • Rodgers, M.T.1    Armentrout, P.B.2
  • 53
    • 0035818138 scopus 로고    scopus 로고
    • Substituent effects in the binding of alkali metal ions to pyridines studied by threshold collision-induced dissociation and ab initio theory: The aminopyridines
    • Rodgers, M.T.: Substituent effects in the binding of alkali metal ions to pyridines studied by threshold collision-induced dissociation and ab initio theory: The aminopyridines. J. Phys. Chem. A 105, 8145-8153 (2001)
    • (2001) J. Phys. Chem. A , vol.105 , pp. 8145-8153
    • Rodgers, M.T.1
  • 54
    • 0003115956 scopus 로고
    • Thermodynamics and mechanism of complexation of peptides with 18-crown-6 in water
    • Kulikov, O.V., Krestov, G.A.: Thermodynamics and mechanism of complexation of peptides with 18-crown-6 in water. Pure Appl. Chem. 67, 1103-1108 (1995)
    • (1995) Pure Appl. Chem. , vol.67 , pp. 1103-1108
    • Kulikov, O.V.1    Krestov, G.A.2
  • 55
    • 0032366914 scopus 로고    scopus 로고
    • Evaluated gas phase basicities and proton affinities of molecules: An update
    • Hunter, E.P., Lias, S.G.: Evaluated gas phase basicities and proton affinities of molecules: An update. J. Phys. Chem. Ref. Data 27, 413-656 (1998)
    • (1998) J. Phys. Chem. Ref. Data , vol.27 , pp. 413-656
    • Hunter, E.P.1    Lias, S.G.2
  • 56
    • 0000978754 scopus 로고
    • He(I) and he(II) photoelectron spectra of glycine and related molecules
    • Cannington, P.H., Ham, N.S.: He(I) and He(II) photoelectron spectra of glycine and related molecules. J. Electron Spectrosc. Relat. Phenom. 32, 139-151 (1983)
    • (1983) J. Electron Spectrosc. Relat. Phenom. , vol.32 , pp. 139-151
    • Cannington, P.H.1    Ham, N.S.2
  • 57
    • 17444402420 scopus 로고    scopus 로고
    • Protonation thermochemistry of alpha-aminoacids bearing a basic residue
    • Bouchoux, G., Buisson, D.A., Colas, C., Sablier, M.: Protonation thermochemistry of alpha-aminoacids bearing a basic residue. Eur. J. Mass Spectrom. 10, 977-992 (2004)
    • (2004) Eur. J. Mass Spectrom. , vol.10 , pp. 977-992
    • Bouchoux, G.1    Buisson, D.A.2    Colas, C.3    Sablier, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.